| Description | All coronaviruses have a similar genomic structure comprising two large open reading frames (ORFs) (ORF1a and ORF1b) encoding the coronavirus replicase. At the 3' end, the genome encodes four structural proteins (S, E, M and N) and a variable number of accessory proteins. Accessory proteins play an important role in virus-host interactions, especially in antagonizing or regulating host immunity and virus adaptation to the host. There are large variations in the number of accessory proteins (1-10) among coronaviruses. Betacoronavirus (bCoVs) have 3-5 accessory proteins, except for SARS-CoV and SARS-CoV-2, which possess the largest number of accessory proteins among all coronaviruses (10 and 9, respectively). 3a-like accessory proteins are found in multiple alpha and betacoronavirus lineages that infect bats and humans. They are transmembrane proteins of the viroporin family that form ion channels in the host membrane and have been implicated in inducing apoptosis, pathogenicity, and virus release. The induction of cytokine storms in COVID-19 patients might be linked to ORF3a mediated activation of inflammasome. 3a-like viroporins contain a transmembrane domain (TM) and a cytosolic domain (CD) [ , , , , , , ].This is the cytosolic domain (CD) of 3a-like viroporins, which consists of two antiparallel β-sheets forming a β-sandwich. The 3a-like viroporin forms a dimer and the six transmembrane helices of the dimer form an ion channel with polar/charged residues in the interior of the channel capable of conducting cations [ ]. | Name | 3a-like viroporin, cytosolic domain, alpha/betacoronavirus |
| Short Name | a/bCoV_VIROPORIN_3A-like_CD | Type | Domain |
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